PMID:21317324

Citation	Camberg, JL, Hoskins, JR and Wickner, S (2011) The interplay of ClpXP with the cell division machinery in Escherichia coli. J. Bacteriol. 193:1911-8
Abstract	ClpXP is a two-component protease composed of ClpX, an ATP-dependent chaperone that recognizes and unfolds specific substrates, and ClpP, a serine protease. One ClpXP substrate in Escherichia coli is FtsZ, which is essential for cell division. FtsZ polymerizes and forms the FtsZ ring at midcell, where division occurs. To investigate the role of ClpXP in cell division, we examined the effects of clpX and clpP deletions in several strains that are defective for cell division. Together, our results suggested that ClpXP modulates cell division through degradation of FtsZ and possibly other cell division components that function downstream of FtsZ ring assembly. In the ftsZ84 strain, which is temperature sensitive for filamentation due to a mutation in ftsZ, we observed that deletion of clpX or clpP suppresses filamentation and reduces FtsZ84 degradation. These results are consistent with ClpXP playing a role in cell division by modulating the level of FtsZ through degradation. In another division-defective strain, ΔminC, the additional deletion of clpX or clpP delays cell division and exacerbates filamentation. Our results demonstrate that ClpXP modulates division in cells lacking MinC by a mechanism that requires ATP-dependent degradation. However, antibiotic chase experiments in vivo indicate that FtsZ degradation is slower in the ΔminC strain than in the wild type, suggesting there may be another cell division component degraded by ClpXP. Taken together these studies suggest that ClpXP may degrade multiple cell division proteins, thereby modulating the precise balance of the components required for division.
Links	PubMed PMC3133021 Online version:10.1128/JB.01317-10
Keywords	Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Bacterial Proteins/metabolism; Cell Division; Cytoskeletal Proteins/metabolism; Endopeptidase Clp/genetics; Endopeptidase Clp/metabolism; Escherichia coli/cytology; Escherichia coli/metabolism; Escherichia coli/physiology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Deletion; Membrane Proteins/genetics; Membrane Proteins/metabolism; Microscopy; Molecular Chaperones/genetics; Molecular Chaperones/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECOLI:FTSZ	involved_in	GO:0051301: cell division	ECO:0000316: genetic interaction evidence used in manual assertion	UniProtKB:P0A6H1	P		Seeded From UniProt	complete
ECOLI:FTSZ	involved_in	GO:0051301: cell division	ECO:0000316: genetic interaction evidence used in manual assertion		P		Seeded From UniProt	Missing: with/from
ECOLI:FTSZ		GO:0051301: cell division	ECO:0000316:	UniProtKB:P0A6H1	P		Fig 1.	complete CACAO 6836
ECOLI:CLPX		GO:0009408: response to heat	ECO:0000315:		P		Fig 1A depletion of clpX surpresses temperature-sensitive filamentation in cells causing them to be shorter.	complete CACAO 4531
ECOLI:CLPX		GO:0051301: cell division	ECO:0000316:	UniProtKB:P0A9A6	P		Fig 1	complete CACAO 6785
ECOLI:CLPX	involved_in	GO:0051301: cell division	ECO:0000316: genetic interaction evidence used in manual assertion		P		Seeded From UniProt	Missing: with/from
ECOLI:CLPX	involved_in	GO:0051301: cell division	ECO:0000316: genetic interaction evidence used in manual assertion	UniProtKB:P0A9A6	P		Seeded From UniProt	complete
ECOLI:CLPP		GO:0009408: response to heat	ECO:0000315:		P		Fig 1A deletion of clpP suppresses temperature-sensitive filamentation cells causing the cells to become elongated.	complete CACAO 4525

References

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